Photochemical initiation of electron transfer reactions.

It is quite apparent that the use of photoinitiated electron transfer has become a powerful, if not dominating, technique in the study of biological electron transfer. It provides a means to measure directly very fast processes and, through the choice of approach (flavin semiquinones or related, metal substitution in hemes or modification with ruthenium) and experimental conditions, provides the ability to probe different features of the electron transfer mechanism. Nevertheless, much remains to be done to fully understand biological electron transfer. The use of photoinitiated electron transfer has clearly established a role for a number of factors involved in controlling the kinetics of electron transfer, including driving force, distance, intervening media, dynamics (conformational gating) and orientation of redox centers. However, we have only scratched the surface in regard to understanding in molecular terms the details of electron transfer in physiologically relevant systems. Thus, even relatively simple and well characterized systems like cytochrome c-cytochrome c peroxidase remain obscure in terms of the through-protein electron paths (intervening media) and the role of protein dynamics in controlling electron transfer kinetics. Indeed, it is the through-protein paths and conformational gating that are unique to biological systems and provide nature with the capability of modulating electron transfer kinetics to optimize biological function. Of the techniques described here, the use of flavin semiquinones is clearly the least invasive in that there is no evidence that flavin semiquinones bind to or perturb physiologically relevant systems. However, this approach is constrained in that precise distances and orientations are not always known, and the range of driving forces available is limited. In contrast, metal substitution and ruthenation allow the positions of interacting redox centers to be reasonably well defined and can provide a very large range of driving force. This latter point is particularly important since it provides a means to discriminate between rate limiting electron transfer and conformational gating. Nevertheless, chemically modifying redox proteins runs the risk of structural and electrostatic alterations which can be difficult to detect but have profound effects on the redox kinetics. Moreover, the intrinsic protein dynamics can be affected, resulting, in the worst case, in changes in conformational gating which cannot be resolved from rate limiting electron transfer. Given the early stage of development of photo-initiated electron transfer, substantial progress can be expected in the next few years. No doubt new approaches will be developed and existing approaches further refined. Especially important, the theoretical basis for interpreting and understanding electron transfer will continue to evolve.(ABSTRACT TRUNCATED AT 400 WORDS)